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Expression regulation of plant ascorbate peroxidase and its tolerance to abiotic stresses

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  • College of Life Sciences, Beijing Normal University, Beijing 100875, China

Received date: 2012-07-09

  Revised date: 2012-11-27

  Online published: 2013-01-25

Abstract

Ascorbate peroxidase (APX), a type I heme peroxidase, catalyzes oxidation of ascorbic acid. It possesses a high degree of specificity to ascorbic acid. APX gene cluster consists of four sub-clusters: the gene clusters of cytosol, chloroplast, mitochondria, and peroxidase. As a key component of hydrogen peroxide detoxification system, the ascorbate-glutathione cycle, APX plays a vital role in the metabolism of H2O2 of plant cells. Studies showed that APX is one of the most important enzymes, which modulate the cellular H2O2 level in redox signaling system. The expression mechanisms of APX isoenzymes are quite complex. Briefly, cytosolic APX is regulated by a variety of signals; two chloroplastic APX isoenzymes are tissue-dependently regulated by alternative splicing. Generated APXs could regulate redox signaling in cells, which further boosts plants tolerance to abiotic stresses. This review focuses on recent advances concerning catalytic properties, physiological function, and gene expressing regulation and abio-stress responding mechanism of APX.

Cite this article

LI Ze-Qin LI Jing-Xiao ZHANG Gen-Fa . Expression regulation of plant ascorbate peroxidase and its tolerance to abiotic stresses[J]. Hereditas(Beijing), 2013 , 35(1) : 45 -54 . DOI: 10.3724/SP.J.1005.2013.00045

References

[1] Mittler R, Vanderauwera S, Suzuki N, Miller G, Tognetti VB, Vandepoele K, Gollery M, Shulaev V, Van Breusegem F. ROS signaling: the new wave? Trends Plant Sci, 2011, 16(6): 300-309.
[2] Mittler R, Vanderauwera S, Gollery M, Van Breusegem F. Reactive oxygen gene network of plants. Trends Plant Sci, 2004, 9(10): 490-498.
[3] 苗雨晨, 白玲, 苗琛, 陈珈, 宋纯鹏. 植物谷胱甘肽过氧化物酶研究进展. 植物学通报, 2005, 22(3): 350-356.
[4] Shigeoka S, Ishikawa T, Tamoi M, Miyagawa Y, Takeda T, Yabuta Y, Yoshimura K. Regulation and function of ascorbate peroxidase isoenzymes. J Exp Bot, 2002, 53(372): 1305-1319.
[5] Panchuk II, Volkov RA, Schoeffl F. Heat stress- and heat shock transcription factor-dependent expression and activity of ascorbate peroxidase in Arabidopsis. Plant Physiol, 2002, 129(2): 838-853.
[6] Narendra S, Venkataramani S, Shen GX, Wang J, Pasapula V, Lin Y, Kornyeyev D, Holaday AS, Zhang H. The Arabidopsis ascorbate peroxidase 3 is a peroxisomal membrane-bound antioxidant enzyme and is dispensable for Arabidopsis growth and development. J Exp Bot, 2006, 57 (12): 3033-3042.
[7] Teixeira FK, Menezes-Benavente L, Margis R, Margis-Pinheiro M. Analysis of the molecular evolutionary his-tory of the ascorbate peroxidase gene family: inferences from the rice genome. J Mol Evol, 2004, 59(6): 761-770.
[8] Teixeira FK, Menezes-Benavente L, Galvão VC, Margis R, Margis-Pinheiro M. Rice ascorbate peroxidase gene family encodes functionally diverse isoforms local-ized in different subcellular compartments. Planta, 2006, 224(2): 300-314.
[9] Yoshimura K, Ishikawa T, Nakamura Y, Tamoi M, Takeda T, Tada T, Nishimura K, Shigeoka S. Comparative study on recombinant chloroplastic and cytosolic ascorbate per-oxidase isozymes of spinach. Arch Biochem Bio-phys, 1998, 353(1): 55-63.
[10] D'arcy-Lameta A, Ferrari-Iliou R, Contour-Ansel1 D, Phamhi AT, Zuily-Fodil Y. Isolation and characteriza-tion of four ascorbate peroxidase cDNAs responsive to water deficit in cowpea leaves. Ann Bot, 2006, 97(1): 133-140.
[11] Welinder KG. Superfamily of plant, fungal and bacterial peroxidases. Curr Opin Struct Biol, 1992, 2(3): 388-393.
[12] Raven EL. Understanding functional diversity and sub-strate specificity in haem peroxidases: what can we learn from ascorbate peroxidase? Nat Prod Rep, 2003, 20(4): 367-381.
[13] Sharp KH, Moody PCE, Brown KA, Raven EL. Crystal structure of the ascorbate peroxidase- salicylhydroxamic acid complex. Biochemistry, 2004, 43(27): 8644-8651.
[14] Sharp KH, Mewies M, Moody PCE, Raven EL. Crystal structure of the ascorbate peroxidase- ascorbate complex. Nat Struct Biol, 2003, 10(4): 303-307.
[15] Lad L, Mewies M, Raven EL. Substrate binding and cata-lytic mechanism in ascorbate peroxidase: Evidence for two ascorbate binding sites. Biochemistry, 2002, 41(46): 13774- 13781.
[16] Macdonald IK, Badyal SK, Ghamsari L, Moody PCE, Raven EL. Interaction of ascorbate peroxidase with sub-strates: A mechanistic and structural analysis. Biochemistry, 2006, 45(25): 7808- 7817.
[17] Barrows TP, Poulos TL. Role of electrostatics and salt bridges in stabilizing the compound I radical in ascorbate peroxidase. Biochemistry, 2005, 44(43): 14062-14068.
[18] Asada K. The water-water cycle in chloroplasts: scaveng-ing of active oxygens and dissipation of excess photons. Annu Rev Plant Physiol Plant Mol Biol, 1999, 50(1): 601-639.
[19] Hwang JE, Lim CJ, Chen H, Je JY, Song C, Lim CO. Overexpression of Arabidopsis Dehydra- tion-Responsive Element-Binding Protein 2C Confers Tolerance to Oxidative Stress. Mol Cells, 2012, 33(2): 135-140.
[20] Larkindale J, Vierling E. Core genome responses involved in acclimation to high temperature. Plant Physiol, 2008, 146(2): 748-761.
[21] Yoshimura K, Y
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